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The VSG C-terminal domain is inaccessible to antibodies on live trypanosomes

In the mammalian host, the Trypanosoma brucei cell surface is covered with a densely packed protein coat of a single protein, the variant surface glycoprotein (VSG). The VSG is believed to shield invariant surface proteins from host antibodies but there is limited information on how far antibodies c...

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Detalles Bibliográficos
Autores principales: Schwede, Angela, Jones, Nicola, Engstler, Markus, Carrington, Mark
Formato: Texto
Lenguaje:English
Publicado: Elsevier/North-Holland Biomedical Press 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3025347/
https://www.ncbi.nlm.nih.gov/pubmed/21074579
http://dx.doi.org/10.1016/j.molbiopara.2010.11.004
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author Schwede, Angela
Jones, Nicola
Engstler, Markus
Carrington, Mark
author_facet Schwede, Angela
Jones, Nicola
Engstler, Markus
Carrington, Mark
author_sort Schwede, Angela
collection PubMed
description In the mammalian host, the Trypanosoma brucei cell surface is covered with a densely packed protein coat of a single protein, the variant surface glycoprotein (VSG). The VSG is believed to shield invariant surface proteins from host antibodies but there is limited information on how far antibodies can penetrate into the VSG monolayer. Here, the VSG surface coat was probed to determine whether it acts as a barrier to binding of antibodies to the membrane proximal VSG C-terminal domain. The binding of C-terminal domain antibodies to VSG221 or VSG118 was compared with antibodies recognising the cognate whole VSGs. The C-terminal VSG domain was inaccessible to antibodies on live cells but not on fixed cells. This provides further evidence that the VSG coat acts as a barrier and protects the cell from antibodies that would otherwise bind to some of the other externally disposed proteins.
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spelling pubmed-30253472011-02-10 The VSG C-terminal domain is inaccessible to antibodies on live trypanosomes Schwede, Angela Jones, Nicola Engstler, Markus Carrington, Mark Mol Biochem Parasitol Short Communication In the mammalian host, the Trypanosoma brucei cell surface is covered with a densely packed protein coat of a single protein, the variant surface glycoprotein (VSG). The VSG is believed to shield invariant surface proteins from host antibodies but there is limited information on how far antibodies can penetrate into the VSG monolayer. Here, the VSG surface coat was probed to determine whether it acts as a barrier to binding of antibodies to the membrane proximal VSG C-terminal domain. The binding of C-terminal domain antibodies to VSG221 or VSG118 was compared with antibodies recognising the cognate whole VSGs. The C-terminal VSG domain was inaccessible to antibodies on live cells but not on fixed cells. This provides further evidence that the VSG coat acts as a barrier and protects the cell from antibodies that would otherwise bind to some of the other externally disposed proteins. Elsevier/North-Holland Biomedical Press 2011-02 /pmc/articles/PMC3025347/ /pubmed/21074579 http://dx.doi.org/10.1016/j.molbiopara.2010.11.004 Text en © 2011 Elsevier B.V. https://creativecommons.org/licenses/by/3.0/ Open Access under CC BY 3.0 (https://creativecommons.org/licenses/by/3.0/) license
spellingShingle Short Communication
Schwede, Angela
Jones, Nicola
Engstler, Markus
Carrington, Mark
The VSG C-terminal domain is inaccessible to antibodies on live trypanosomes
title The VSG C-terminal domain is inaccessible to antibodies on live trypanosomes
title_full The VSG C-terminal domain is inaccessible to antibodies on live trypanosomes
title_fullStr The VSG C-terminal domain is inaccessible to antibodies on live trypanosomes
title_full_unstemmed The VSG C-terminal domain is inaccessible to antibodies on live trypanosomes
title_short The VSG C-terminal domain is inaccessible to antibodies on live trypanosomes
title_sort vsg c-terminal domain is inaccessible to antibodies on live trypanosomes
topic Short Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3025347/
https://www.ncbi.nlm.nih.gov/pubmed/21074579
http://dx.doi.org/10.1016/j.molbiopara.2010.11.004
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